An Integrated Framework Advancing Membrane Protein Modeling and Design
Fig 5
Structures of mutant residues at position 210 of OmpLA.
(A) The charged residues arginine and lysine (superimposed) cannot reach the interface region. The z-coordinate shows the difference in membrane depth of the two charged side chains. Membrane environment scores are unfavorable for both, with lysine being slightly more unfavorable. (B) Insertion of threonine at position 210 is penalized by a mild clash from the neighboring leucine 225; serine at this position is accommodated more easily (Fig D in S1 File). (C) The tryptophan side chain is close to the neighboring leucine 197, resulting in large repulsive scores. All aromatic mutations have a comparably large repulsive van der Waals and rotamer scores, resulting in over-prediction of their ΔΔG values.